Evidence map›Paper›PMID 26896802›Full record

ArticleNucleic acids research2016

Mechanism of DNA loading by the DNA repair helicase XPD.

Diana Constantinescu-Aruxandei, Biljana Petrovic-Stojanovska, J Carlos Penedo, Malcolm F White, James H Naismith

Open access · goldAbstract read
In one paragraph

Article in Nucleic acids research, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 30 papers.

0numbers the graph read from it
0cells of the map it votes in
30citing papers in PubMed
4.4field-weighted citation impact, top 5% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

30 citing papers in PubMed, 47 citations in OpenAlex.

  1. Article
  2. Review
  3. Article
  4. Review
  5. A new crystal form of the DNA-free full-length XPD helicase from Thermoplasma acidophilum.Acta crystallographica. Section F, Structural biology communications · 2026
    Article
  6. Article
  7. Article
  8. Review
  9. Structure, function and evolution of the bacterial DinG-like proteins.Computational and structural biotechnology journal · 2025
    Review
  10. Article
  11. Article
  12. Review
  13. Mechanism of action of nucleotide excision repair machinery.Biochemical Society transactions · 2022
    Review
  14. Article
  15. Article
  16. Article
  17. Review
  18. Article
  19. Review
  20. Asymmetric base-pair opening drives helicase unwinding dynamics.Proceedings of the National Academy of Sciences of the United States of America · 2019
    Article
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

5 authors at 1 institution in 1 country.

Diana Constantinescu-AruxandeiBiomedical Sciences Research Complex, University of St Andrews, Fife KY16 9ST, UK.
Biljana Petrovic-StojanovskaBiomedical Sciences Research Complex, University of St Andrews, Fife KY16 9ST, UK.
J Carlos PenedoBiomedical Sciences Research Complex, University of St Andrews, Fife KY16 9ST, UK.
Malcolm F WhiteBiomedical Sciences Research Complex, University of St Andrews, Fife KY16 9ST, UK mfw2@st-andrews.ac.uk.
James H NaismithBiomedical Sciences Research Complex, University of St Andrews, Fife KY16 9ST, UK naismith@st-andrews.ac.uk.
University of St Andrews · GB

Funding

Wellcome Trust 099149/Z/12/ZWellcome Trust WT091825MA
6 · The paper itself

Abstract

The xeroderma pigmentosum group D (XPD) helicase is a component of the transcription factor IIH complex in eukaryotes and plays an essential role in DNA repair in the nucleotide excision repair pathway. XPD is a 5' to 3' helicase with an essential iron-sulfur cluster. Structural and biochemical studies of the monomeric archaeal XPD homologues have aided a mechanistic understanding of this important class of helicase, but several important questions remain open. In particular, the mechanism for DNA loading, which is assumed to require large protein conformational change, is not fully understood. Here, DNA binding by the archaeal XPD helicase from Thermoplasma acidophilum has been investigated using a combination of crystallography, cross-linking, modified substrates and biochemical assays. The data are consistent with an initial tight binding of ssDNA to helicase domain 2, followed by transient opening of the interface between the Arch and 4FeS domains, allowing access to a second binding site on helicase domain 1 that directs DNA through the pore. A crystal structure of XPD from Sulfolobus acidocaldiarius that lacks helicase domain 2 has an otherwise unperturbed structure, emphasizing the stability of the interface between the Arch and 4FeS domains in XPD.

Indexed as

DNA RepairAmino Acid MotifsArchaeal ProteinsBinding SitesCloning, MolecularCrystallography, X-RayDNA, ArchaealDNA DamageDNA, Single-StrandedEscherichia coliGene ExpressionModels, MolecularMolecular Sequence DataProtein BindingProtein StabilityProtein Structure, SecondaryArchaeal ProteinsDNA, ArchaealDNA, Single-StrandedRecombinant ProteinsXeroderma Pigmentosum Group D Protein

Identifiers

PMID26896802
PMCPMC4824113
OpenAlexW2275177904

What OpenQuestion holds

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LicenceCC BY
Read underepoch 390

Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.